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Molecular properties of the matrixprotein(M) gene of the lapinized rinderpest virus

M Shiotani1, R Miura, K Fujita

  • 1Laboratory of Animal Research Center, Institute of Medical Science, The University of Tokyo, Japan.

The Journal of Veterinary Medical Science
|August 16, 2001
PubMed

Insights

The matrix protein (M) gene sequence of lapinized rinderpest virus (RPV-L) was determined. This M protein shows high amino acid homology with other morbilliviruses, aiding in rinderpest virus research.

Area of Science:

  • Virology
  • Molecular Biology
  • Genetics

Background:

  • Rinderpest virus (RPV) is a highly contagious disease affecting cattle.
  • Understanding the genetic makeup of RPV strains, including lapinized variants, is crucial for disease control and vaccine development.
  • The matrix protein (M) plays a vital role in virus assembly and is a conserved protein among morbilliviruses.

Purpose of the Study:

  • To determine the complete nucleotide sequence of the matrix protein (M) gene of the lapinized rinderpest virus (RPV-L).
  • To analyze the predicted amino acid sequence of the RPV-L M protein and compare its homology with other morbilliviruses.

Main Methods:

  • Nucleotide sequencing of the full-length cDNA of the RPV-L M gene.
  • Bioinformatic analysis to predict the amino acid sequence and calculate homology with related viruses.

Main Results:

  • The full-length cDNA of the RPV-L M gene is 1460 base pairs, encoding a 335-amino acid M protein.
  • The predicted amino acid sequence of RPV-L M protein exhibits high homology (94% with RPV Kabete 'O', 93% with RPV RBOK strain) to other rinderpest virus strains.
  • Significant homology was also observed with measles virus (87%) and canine distemper virus (77%).

Conclusions:

  • The complete coding region of the RPV-L strain's M gene has been elucidated.
  • The high sequence homology supports the classification of RPV-L within the morbillivirus genus and provides insights into conserved regions important for viral function.

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